Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Targeting of the N-terminal coiled coil oligomerization interface of BCR interferes with the transformation potential of BCR-ABL and increases sensitivity to STI571.

Blood - 15 Oct 2003

Beissert Tim, Puccetti Elena, Bianchini Andrea, Güller Saskia, Boehrer Simone, Hoelzer Dieter, Ottmann Oliver Gerhard, Nervi Clara, Ruthardt Martin

Abstract excerpt

Translocations involving the abl locus on chromosome 9 fuses the tyrosine kinase c-ABL to proteins harboring oligomerization interfaces such as BCR or TEL, enabling these ABL-fusion proteins (X-ABL) to transform cells and to induce leukemia. The ABL kinase activity is blocked by the ABL kinase inhibitor STI571 which abrogates transformation by X-ABL. To investigate the role of oligomerization for the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Benzamides
Share to Fusion Proteins, bcr-abl

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Imatinib Mesylate

Share to Inhibitory Concentration 50

Share to Leukemia

Share to Oncogene Proteins

Share to Piperazines

Share to Retroviridae

Source

Identifiers

PMID: 12829585
DOI: 10.1182/blood-2003-03-0811

Genes

BCR
PML

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeting of the N-terminal coiled coil oligomerization interface of BCR interferes with the transformation potential of BCR-ABL and increases sensitivity to STI571.PMID 12829585Read ↗

A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins.Semantic proximity Read ↗

Targeting of the N-terminal coiled coil oligomerization interface by a helix-2 peptide inhibits unmutated and imatinib-resistant BCR/ABL.Semantic proximity Read ↗

Autoinhibition of Bcr-Abl through its SH3 domain.Semantic proximity Read ↗

The SH2-containing adapter protein GRB10 interacts with BCR-ABL.Semantic proximity Read ↗

Analysis of the Structural Basis of Specificity of Inhibition of the Abl Kinase by STI571Semantic proximity Read ↗

Oligomerization of the ABL Tyrosine Kinase by the Ets Protein TEL in Human LeukemiaSemantic proximity Read ↗

Temperature-sensitive transformation by an Abelson virus mutant encoding an altered SH2 domain.Semantic proximity Read ↗

Improved Coiled-Coil Design Enhances Interaction with Bcr-Abl and Induces ApoptosisSemantic proximity Read ↗

c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines.Semantic proximity Read ↗

Bcr/Abl activates transcription of theBcl-X gene through STAT5Semantic proximity Read ↗

Deletion of the Src Homology 3 Domain and C-terminal Proline-rich Sequences in Bcr-Abl Prevents Abl Interactor 2 Degradation and Spontaneous Cell Migration and Impairs LeukemogenesisSemantic proximity Read ↗

Peptide containing the BCR oligomerization domain (AA 1-160) reverses the transformed phenotype of p210bcr-abl positive 32D myeloid leukemia cells.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.